Abstract
1. The effects of temperature on the catalytic and regulatory properties of pyruvate kinases from the temperate-zone rainbow trout and the Antarctic fish Trematomus bernacchii were examined. 2. The K(m) value of pyruvate kinase for one of its two substrates, phosphoenolpyruvate, is temperature-dependent, and is lowest at temperatures that closely coincide with the habitat temperatures of the two fishes. 3. Two regulatory functions of pyruvate kinase, feedforward activation by fructose diphosphate and feedback inhibition by ATP, are temperature-independent. Enzyme-ADP interaction is also temperature-independent. 4. It is concluded that enzyme-substrate and enzyme-modulator interactions are important factors in short-term and in evolutionary adaptations by poikilotherms to changes in temperature. Though the K(m) for substrate may vary in apparently adaptive manners, the regulatory functions of an enzyme appear to be unchanged over the range of temperatures experienced by the organism in Nature.
MeSH Terms
Adaptation, Physiological
Adenine Nucleotides/metabolism
Animals
Body Temperature
Cold Climate
Feedback
Fishes/metabolism
Isoenzymes
Kinetics
Muscles/enzymology
Pyruvate Kinase/metabolism
Pyruvates/metabolism
Salmonidae/metabolism
Temperature
Chemicals
Adenine Nucleotides
Isoenzymes
Pyruvates
Pyruvate Kinase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Somero G N
Hochachka P W
References (15)
15 references, click to expand
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